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Literature DB >> 21764920

The endolysin-binding domain encompasses the N-terminal region of the mycobacteriophage Ms6 Gp1 chaperone.

Maria João Catalão¹, Filipa Gil, José Moniz-Pereira, Madalena Pimentel.

Abstract

The intermolecular interactions of the mycobacteriophage Ms6 secretion chaperone with endolysin were characterized. The 384-amino-acid lysin (lysin(384))-binding domain was found to encompass the N-terminal region of Gp1, which is also essential for a lysis phenotype in Escherichia coli. In addition, a GXXXG-like motif involved in Gp1 homo-oligomerization was identified within the C-terminal region.

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Year: 2011 PMID： 21764920 PMCID： PMC3165679 DOI： 10.1128/JB.00380-11

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

18 in total

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Authors: Miguel Garcia; Madalena Pimentel; José Moniz-Pereira
Journal: J Bacteriol Date: 2002-06 Impact factor: 3.490

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Journal: J Mol Biol Date: 2000-02-25 Impact factor: 5.469

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Authors: Dirk Schneider; Donald M Engelman
Journal: J Mol Biol Date: 2004-10-29 Impact factor: 5.469

10. A second endolysin gene is fully embedded in-frame with the lysA gene of mycobacteriophage Ms6.

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Journal: PLoS One Date: 2011-06-09 Impact factor: 3.240

7 in total

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7. Insight into the Lytic Functions of the Lactococcal Prophage TP712.

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7 in total